Atrolysin E

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Atrolysin E
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EC no. 3.4.24.44
CAS no. 172306-51-3
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Atrolysin E (EC 3.4.24.44, Crotalus atrox metalloendopeptidase e, hemorrhagic toxin e) is an enzyme. [1] [2] [3] This enzyme catalyses the following chemical reaction

Cleavage of Asn3-Gln, Ser9-His and Ala14-Leu bonds in insulin B chain and Tyr14-Gln and Thr8-Ser in A chain. Cleaves type IV collagen at Ala73-Gln in alpha1(IV) and at Gly7-Leu in alpha2(IV)

This endopeptidase is present in the venom of the western diamondback rattlesnake ( Crotalus atrox ).

Related Research Articles

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<i>Crotalus scutulatus</i> Species of snake

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<span class="mw-page-title-main">Eastern diamondback rattlesnake</span> Species of reptile endemic to the southeastern US

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<span class="mw-page-title-main">Convulxin</span>

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<span class="mw-page-title-main">Western diamondback rattlesnake</span> Species of snake

The western diamondback rattlesnake or Texas diamond-back is a rattlesnake species and member of the viper family, found in the southwestern United States and Mexico. Like all other rattlesnakes and all other vipers, it is venomous. It is likely responsible for the majority of snakebite fatalities in northern Mexico and the greatest number of snakebites in the U.S. No subspecies are currently recognized.

Adamalysin is an enzyme. This enzyme catalyses the following chemical reaction

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Crotamine is a toxin present in the venom of the South American rattlesnake. It is a 42-residue long protein containing 11 basic residues and 6 cysteines. It has also been isolated from the venom of North American prairie rattlesnake, Crotalus viridis viridis. It was first isolated and purified by Brazilian scientist José Moura Gonçalves, and later intensively studied by his group of collaborators at the Medical School of Ribeirão Preto of the University of São Paulo.

Venombin A is an enzyme. This enzyme catalyses the following chemical reaction

Atrolysin A is an enzyme that is one of six hemorrhagic toxins found in the venom of western diamondback rattlesnake. This endopeptidase has a length of 419 amino acid residues. The metalloproteinase disintegrin-like domain and the cysteine-rich domain of the enzyme are responsible for the enzyme's hemorrhagic effects on organisms via inhibition of platelet aggregation.

Bothropasin is an enzyme. This enzyme catalyses the following chemical reaction

Atrolysin B is an enzyme. This enzyme catalyses the following chemical reaction

Atrolysin C is an enzyme. This enzyme catalyses the following chemical reaction

Atroxase is an enzyme. This enzyme catalyses the following chemical reaction

Atrolysin F is an enzyme. This enzyme catalyses the following chemical reaction

Horrilysin is an enzyme. This enzyme catalyses the following chemical reaction

Ruberlysin is an enzyme. This enzyme catalyses the following chemical reaction

Trimerelysin II is an enzyme. This enzyme catalyses the following chemical reaction

Fibrolase is an enzyme. This enzyme catalyses the following chemical reaction

References

  1. Bjarnason JB, Tu AT (August 1978). "Hemorrhagic toxins from Western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e". Biochemistry. 17 (16): 3395–404. doi:10.1021/bi00609a033. PMID   210790.
  2. Bjarnason JB, Fox JW (August 1983). "Proteolytic specificity and cobalt exchange of hemorrhagic toxin e, a zinc protease isolated from the venom of the western diamondback rattlesnake (Crotalus atrox)". Biochemistry. 22 (16): 3770–8. doi:10.1021/bi00285a009. PMID   6351911.
  3. Baramova EN, Shannon JD, Bjarnason JB, Fox JW (May 1990). "Identification of the cleavage sites by a hemorrhagic metalloproteinase in type IV collagen". Matrix. 10 (2): 91–7. doi:10.1016/s0934-8832(11)80175-7. PMID   2374521.